ID A0A068R026_9GAMM Unreviewed; 333 AA.
AC A0A068R026;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=tRNA-modifying protein YgfZ {ECO:0000256|HAMAP-Rule:MF_01175};
GN ORFNames=XPG1_0749 {ECO:0000313|EMBL:CDG20404.1};
OS Xenorhabdus poinarii G6.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=1354304 {ECO:0000313|EMBL:CDG20404.1, ECO:0000313|Proteomes:UP000032735};
RN [1] {ECO:0000313|EMBL:CDG20404.1, ECO:0000313|Proteomes:UP000032735}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G6 {ECO:0000313|EMBL:CDG20404.1,
RC ECO:0000313|Proteomes:UP000032735};
RA Genoscope - CEA;
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Folate-binding protein involved in regulating the level of
CC ATP-DnaA and in the modification of some tRNAs. It is probably a key
CC factor in regulatory networks that act via tRNA modification, such as
CC initiation of chromosomal replication. {ECO:0000256|HAMAP-
CC Rule:MF_01175}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01175}.
CC -!- SIMILARITY: Belongs to the tRNA-modifying YgfZ family.
CC {ECO:0000256|HAMAP-Rule:MF_01175}.
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DR EMBL; FO704551; CDG20404.1; -; Genomic_DNA.
DR RefSeq; WP_045957835.1; NZ_FO704551.1.
DR AlphaFoldDB; A0A068R026; -.
DR STRING; 1354304.XPG1_0749; -.
DR KEGG; xpo:XPG1_0749; -.
DR HOGENOM; CLU_007884_6_1_6; -.
DR OrthoDB; 9796287at2; -.
DR Proteomes; UP000032735; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005542; F:folic acid binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009451; P:RNA modification; IEA:InterPro.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-UniRule.
DR Gene3D; 2.40.30.160; -; 1.
DR Gene3D; 3.30.70.1630; -; 1.
DR Gene3D; 3.30.70.1400; Aminomethyltransferase beta-barrel domains; 1.
DR HAMAP; MF_01175; tRNA_modifying_YgfZ; 1.
DR InterPro; IPR029043; GcvT/YgfZ_C.
DR InterPro; IPR023758; tRNA-modifying_YgfZ.
DR InterPro; IPR045179; YgfZ/GcvT.
DR InterPro; IPR017703; YgfZ/GcvT_CS.
DR InterPro; IPR048451; YgfZ_barrel.
DR NCBIfam; TIGR03317; ygfZ_signature; 1.
DR PANTHER; PTHR22602:SF0; TRANSFERASE CAF17, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR22602; UNCHARACTERIZED; 1.
DR Pfam; PF21130; YgfZ_barrel; 1.
DR SUPFAM; SSF101790; Aminomethyltransferase beta-barrel domain; 1.
DR SUPFAM; SSF103025; Folate-binding domain; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01175};
KW Folate-binding {ECO:0000256|ARBA:ARBA00022954, ECO:0000256|HAMAP-
KW Rule:MF_01175};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_01175}.
FT DOMAIN 248..315
FT /note="tRNA-modifying protein YgfZ-like beta-barrel"
FT /evidence="ECO:0000259|Pfam:PF21130"
FT BINDING 28
FT /ligand="folate"
FT /ligand_id="ChEBI:CHEBI:62501"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01175"
FT BINDING 192
FT /ligand="folate"
FT /ligand_id="ChEBI:CHEBI:62501"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01175"
SQ SEQUENCE 333 AA; 36884 MW; 7336A8F845E21775 CRC64;
MAYQIPFSAQ YPSPSATLPL TLISLDDWGI VTVIGSDTEK YLQGQVTADL TALNDNQHVL
TAHCDAKGKM WSNLRLFQRG EGFAYIERRS LLETQLTELK KYAVFSKVTF VNDEESVLLG
VAGKGSRAAL ATHFPTLPDT ESSVIQHGTT TLLHFALPAE RFLLMTDKTT AATLTQTFVE
EYQSQLNNSQ QWLALEIEAG IPVIDAASSA QFIPQATNLQ AIENSISFKK GCYTGQEMVA
RAKYRGANKR AMYWLAGSAS SLPVAGDDLE WQLGDKWRRT GSVLAAVKLV DGSIWVQVVM
NNDMELESVF RIREDENSML TIQALPYSLD EEK
//
